메뉴 건너뛰기




Volumn 86, Issue 2, 2012, Pages

Ontogeny of aquaporins in human fetal membranes1

Author keywords

Aquaporin; Fetal membranes; Gene expression; Human reproduction; Placenta; Placental transport

Indexed keywords

AQUAPORIN; AQUAPORIN 1; AQUAPORIN 11; AQUAPORIN 3; AQUAPORIN 8; AQUAPORIN 9; MESSENGER RNA; UNCLASSIFIED DRUG; AQP11 PROTEIN, HUMAN; AQP9 PROTEIN, HUMAN;

EID: 84860249012     PISSN: 00063363     EISSN: 15297268     Source Type: Journal    
DOI: 10.1095/biolreprod.111.095448     Document Type: Article
Times cited : (40)

References (38)
  • 1
    • 0034777628 scopus 로고    scopus 로고
    • Use of transgenic mice model for understanding the placentation: towards clinical applications in human obstetrical pathologies?
    • Sapin V, Blanchon L, Serre AF, Lemery D, Dastugue B, Ward SJ. Use of transgenic mice model for understanding the placentation: towards clinical applications in human obstetrical pathologies? Transgenic Res 2001; 10:377-398.
    • (2001) Transgenic Res , vol.10 , pp. 377-398
    • Sapin, V.1    Blanchon, L.2    Serre, A.F.3    Lemery, D.4    Dastugue, B.5    Ward, S.J.6
  • 2
    • 0030748555 scopus 로고    scopus 로고
    • Physiology of amniotic fluid volume regulation
    • Brace RA. Physiology of amniotic fluid volume regulation. Clin Obstet Gynecol 1997; 40:280-289.
    • (1997) Clin Obstet Gynecol , vol.40 , pp. 280-289
    • Brace, R.A.1
  • 3
    • 47349119183 scopus 로고    scopus 로고
    • Amniotic fluid abnormalities
    • Harman CR. Amniotic fluid abnormalities. Semin Perinatol 2008; 32:288-294.
    • (2008) Semin Perinatol , vol.32 , pp. 288-294
    • Harman, C.R.1
  • 5
    • 0028318868 scopus 로고
    • Molecular structure of the water channel through aquaporin CHIP: the hourglass model
    • Jung JS, Preston GM, Smith BL, Guggino WB, Agre P. Molecular structure of the water channel through aquaporin CHIP: the hourglass model. J Biol Chem 1994; 269:14648-14654.
    • (1994) J Biol Chem , vol.269 , pp. 14648-14654
    • Jung, J.S.1    Preston, G.M.2    Smith, B.L.3    Guggino, W.B.4    Agre, P.5
  • 9
    • 0037131175 scopus 로고    scopus 로고
    • Characterization of aquaporin-6 as a nitrate channel in mammalian cells: requirement of pore-lining residue threonine 63
    • Ikeda M, Beitz E, Kozono D, Guggino WB, Agre P, Yasui M. Characterization of aquaporin-6 as a nitrate channel in mammalian cells: requirement of pore-lining residue threonine 63. J Biol Chem 2002; 277:39873-39879.
    • (2002) J Biol Chem , vol.277 , pp. 39873-39879
    • Ikeda, M.1    Beitz, E.2    Kozono, D.3    Guggino, W.B.4    Agre, P.5    Yasui, M.6
  • 10
    • 0026332210 scopus 로고
    • Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family
    • Preston GM, Agre P. Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family. Proc Natl Acad Sci U S A 1991; 88:11110-11114.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 11110-11114
    • Preston, G.M.1    Agre, P.2
  • 11
    • 4444221676 scopus 로고    scopus 로고
    • From structure to disease: the evolving tale of aquaporin biology
    • King LS, Kozono D, Agre P. From structure to disease: the evolving tale of aquaporin biology. Nat Rev Mol Cell Biol 2004; 5:687-698.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 687-698
    • King, L.S.1    Kozono, D.2    Agre, P.3
  • 12
    • 0035992790 scopus 로고    scopus 로고
    • Physiological importance of aquaporin water channels
    • Verkman AS. Physiological importance of aquaporin water channels. Ann Med 2002; 34:192-200.
    • (2002) Ann Med , vol.34 , pp. 192-200
    • Verkman, A.S.1
  • 13
    • 79952006809 scopus 로고    scopus 로고
    • Review: water channel proteins in the human placenta and fetal membranes
    • Damiano AE. Review: water channel proteins in the human placenta and fetal membranes. Placenta 2011; 32(suppl 2):S207-S211.
    • (2011) Placenta , vol.32 , Issue.SUPPL. 2
    • Damiano, A.E.1
  • 14
    • 77955138270 scopus 로고    scopus 로고
    • Retinoids regulate human amniotic tissue-type plasminogen activator gene by a two-step mechanism
    • Borel V, Marceau G, Gallot D, Blanchon L, Sapin V. Retinoids regulate human amniotic tissue-type plasminogen activator gene by a two-step mechanism. J Cell Mol Med 2010; 14(6B):1793-1805.
    • (2010) J Cell Mol Med , vol.14 , Issue.6 B , pp. 1793-1805
    • Borel, V.1    Marceau, G.2    Gallot, D.3    Blanchon, L.4    Sapin, V.5
  • 18
    • 51249112755 scopus 로고    scopus 로고
    • Aquaporins and fetal fluid balance
    • Liu H, Zheng Z, Wintour EM. Aquaporins and fetal fluid balance. Placenta 2008; 29:840-847.
    • (2008) Placenta , vol.29 , pp. 840-847
    • Liu, H.1    Zheng, Z.2    Wintour, E.M.3
  • 20
    • 0024447789 scopus 로고
    • The missing link in amniotic fluid volume regulation: intramembranous absorption
    • Gilbert WM, Brace RA. The missing link in amniotic fluid volume regulation: intramembranous absorption. Obstet Gynecol 1989; 74:748-754.
    • (1989) Obstet Gynecol , vol.74 , pp. 748-754
    • Gilbert, W.M.1    Brace, R.A.2
  • 22
    • 34247172121 scopus 로고    scopus 로고
    • Placental and membrane aquaporin water channels: correlation with amniotic fluid volume and composition
    • Beall MH, Wang S, Yang B, Chaudhri N, Amidi F, Ross MG. Placental and membrane aquaporin water channels: correlation with amniotic fluid volume and composition. Placenta 2007; 28:421-428.
    • (2007) Placenta , vol.28 , pp. 421-428
    • Beall, M.H.1    Wang, S.2    Yang, B.3    Chaudhri, N.4    Amidi, F.5    Ross, M.G.6
  • 24
    • 0030748555 scopus 로고    scopus 로고
    • Physiology of amniotic fluid volume regulation
    • Brace RA. Physiology of amniotic fluid volume regulation. Clin Obstet Gynecol 1997; 40:289-282.
    • (1997) Clin Obstet Gynecol , vol.40 , pp. 289-282
    • Brace, R.A.1
  • 25
    • 10044276702 scopus 로고    scopus 로고
    • Expression of aquaporin 9 in human chorioamniotic membranes and placenta
    • Wang S, Chen J, Beall M, Zhou W, Ross MG. Expression of aquaporin 9 in human chorioamniotic membranes and placenta. Am J Obstet Gynecol 2004; 191:2160-2167.
    • (2004) Am J Obstet Gynecol , vol.191 , pp. 2160-2167
    • Wang, S.1    Chen, J.2    Beall, M.3    Zhou, W.4    Ross, M.G.5
  • 27
    • 0038405295 scopus 로고    scopus 로고
    • Expression of aquaporin 8 and its upregulation by cyclic adenosine monophosphate in human WISH cells
    • Wang S, Chen J, Au KT, Ross MG. Expression of aquaporin 8 and its upregulation by cyclic adenosine monophosphate in human WISH cells. Am J Obstet Gynecol 2003; 188:997-1001.
    • (2003) Am J Obstet Gynecol , vol.188 , pp. 997-1001
    • Wang, S.1    Chen, J.2    Au, K.T.3    Ross, M.G.4
  • 28
    • 0002337089 scopus 로고
    • The establishment of a line (WISH) of human amnion cells in continuous cultivation
    • Hayflick L. The establishment of a line (WISH) of human amnion cells in continuous cultivation. Exp Cell Res 1961; 23:14-20.
    • (1961) Exp Cell Res , vol.23 , pp. 14-20
    • Hayflick, L.1
  • 29
    • 20444441230 scopus 로고    scopus 로고
    • A novel model of polyhydramnios: amniotic fluid volume is increased in aquaporin 1 knockout mice
    • Mann SE, Ricke EA, Torres EA, Taylor RN. A novel model of polyhydramnios: amniotic fluid volume is increased in aquaporin 1 knockout mice. Am J Obstet Gynecol 2005; 192:2041-2046.
    • (2005) Am J Obstet Gynecol , vol.192 , pp. 2041-2046
    • Mann, S.E.1    Ricke, E.A.2    Torres, E.A.3    Taylor, R.N.4
  • 30
    • 0031786931 scopus 로고    scopus 로고
    • Role of aquaporin water channels in kidney and lung
    • Verkman AS. Role of aquaporin water channels in kidney and lung. Am J Med Sci 1998; 316:310-320.
    • (1998) Am J Med Sci , vol.316 , pp. 310-320
    • Verkman, A.S.1
  • 31
    • 33748560815 scopus 로고    scopus 로고
    • Aquaporin subfamily with unusual NPA boxes
    • Ishibashi K. Aquaporin subfamily with unusual NPA boxes. Biochim Biophys Acta 2006; 1758:989-993.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 989-993
    • Ishibashi, K.1
  • 32
    • 33744978147 scopus 로고    scopus 로고
    • Aquaporin-11: a channel protein lacking apparent transport function expressed in brain
    • Gorelick DA, Praetorius J, Tsunenari T, Nielsen S, Agre P. Aquaporin-11: a channel protein lacking apparent transport function expressed in brain. BMC Biochem 2006; 7
    • (2006) BMC Biochem , pp. 7
    • Gorelick, D.A.1    Praetorius, J.2    Tsunenari, T.3    Nielsen, S.4    Agre, P.5
  • 35
    • 79954424212 scopus 로고    scopus 로고
    • Water permeability and characterization of aquaporin-11
    • Yakata K, Tani K, Fujiyoshi Y. Water permeability and characterization of aquaporin-11. J Struct Biol 2011; 174:315-320.
    • (2011) J Struct Biol , vol.174 , pp. 315-320
    • Yakata, K.1    Tani, K.2    Fujiyoshi, Y.3
  • 36
    • 54049149970 scopus 로고    scopus 로고
    • Aquaporin-11 knockout mice and polycystic kidney disease animals share a common mechanism of cyst formation
    • Okada S, Misaka T, Tanaka Y, Matsumoto I, Ishibashi K, Sasaki S, Abe K. Aquaporin-11 knockout mice and polycystic kidney disease animals share a common mechanism of cyst formation. FASEB J 2008; 22:3672-3684.
    • (2008) FASEB J , vol.22 , pp. 3672-3684
    • Okada, S.1    Misaka, T.2    Tanaka, Y.3    Matsumoto, I.4    Ishibashi, K.5    Sasaki, S.6    Abe, K.7
  • 37
    • 77952760166 scopus 로고    scopus 로고
    • Expression of aquaporin-1 in human oligohydramnios placenta and fetal membranes [in Chinese]
    • Hao RZ, Liu HS, Xiong ZF. Expression of aquaporin-1 in human oligohydramnios placenta and fetal membranes [in Chinese]. Nan Fang Yi Ke Da Xue Xue Bao 2009; 29:1130-1132.
    • (2009) Nan Fang Yi Ke Da Xue Xue Bao , vol.29 , pp. 1130-1132
    • Hao, R.Z.1    Liu, H.S.2    Xiong, Z.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.